YIL124W - Revision history

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{{PageTop}}
{|{{Prettytable}} align = 'right' width = '200px'
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YIL124W YIL124W]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''AYR1 ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||'' ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr IX:126204..127097
|-
|colspan = '3'|{{Don'tEditThisBox}}
|}
 
'''Description of {{PAGENAME}}:''' NADPH-dependent 1-acyl dihydroxyacetone phosphate reductase found in lipid particles, ER, and mitochondrial outer membrane; involved in phosphatidic acid biosynthesis; required for spore germination; capable of metabolizing steroid hormones<ref name='S000114057'>Zahedi RP, et al. (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol Biol Cell 17(3):1436-50 {{SGDpaper|S000114057}} PMID 16407407</ref><ref name='S000070219'>Vico P, et al. (2002) Dehydroepiandrosterone (DHEA) metabolism in Saccharomyces cerevisiae expressing mammalian steroid hydroxylase CYP7B: Ayr1p and Fox2p display 17beta-hydroxysteroid dehydrogenase activity. Yeast 19(10):873-86 {{SGDpaper|S000070219}} PMID 12112241</ref><ref name='S000055653'>Athenstaedt K and Daum G (2000) 1-Acyldihydroxyacetone-phosphate reductase (Ayr1p) of the yeast Saccharomyces cerevisiae encoded by the open reading frame YIL124w is a major component of lipid particles. J Biol Chem 275(1):235-40
{{SGDpaper|S000055653}} PMID 10617610</ref>
 
 
 
 

__TOC__
==Community Commentary==
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==References==

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@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YIL124W:''' NADPH-dependent 1-acyl dihydroxyacetone phosphate reductase found in lipid particles, ER, and mitochondrial outer membrane; involved in phosphatidic acid biosynthesis; required for spore germination; capable of metabolizing steroid hormones<ref name='S000055653'>Athenstaedt K and Daum G (2000) 1-Acyldihydroxyacetone-phosphate reductase (Ayr1p) of the yeast Saccharomyces cerevisiae encoded by the open reading frame YIL124w is a major component of lipid particles. J Biol Chem 275(1):235-40 {{SGDpaper|S000055653}} PMID 10617610</ref><ref name='S000114057'>Zahedi RP, et al. (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol Biol Cell 17(3):1436-50 {{SGDpaper|S000114057}} PMID 16407407</ref><ref name='S000070219'>Vico P, et al. (2002) Dehydroepiandrosterone (DHEA) metabolism in Saccharomyces cerevisiae expressing mammalian steroid hydroxylase CYP7B: Ayr1p and Fox2p display 17beta-hydroxysteroid dehydrogenase activity. Yeast 19(10):873-86
+'''Description of YIL124W:''' NADPH-dependent 1-acyl dihydroxyacetone phosphate reductase found in lipid particles, ER, and mitochondrial outer membrane; involved in phosphatidic acid biosynthesis; required for spore germination; capable of metabolizing steroid hormones<ref name='S000055653'>Athenstaedt K and Daum G (2000) 1-Acyldihydroxyacetone-phosphate reductase (Ayr1p) of the yeast Saccharomyces cerevisiae encoded by the open reading frame YIL124w is a major component of lipid particles. J Biol Chem 275(1):235-40 {{SGDpaper|S000055653}} PMID 10617610</ref><ref name='S000070219'>Vico P, et al. (2002) Dehydroepiandrosterone (DHEA) metabolism in Saccharomyces cerevisiae expressing mammalian steroid hydroxylase CYP7B: Ayr1p and Fox2p display 17beta-hydroxysteroid dehydrogenase activity. Yeast 19(10):873-86 {{SGDpaper|S000070219}} PMID 12112241</ref><ref name='S000114057'>Zahedi RP, et al. (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol Biol Cell 17(3):1436-50
-  {{SGDpaper|S000070219}} PMID 12112241</ref>
+  {{SGDpaper|S000114057}} PMID 16407407</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YIL124W:''' NADPH-dependent 1-acyl dihydroxyacetone phosphate reductase found in lipid particles, ER, and mitochondrial outer membrane; involved in phosphatidic acid biosynthesis; required for spore germination; capable of metabolizing steroid hormones<ref name='S000114057'>Zahedi RP, et al. (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol Biol Cell 17(3):1436-50 {{SGDpaper|S000114057}} PMID 16407407</ref><ref name='S000070219'>Vico P, et al. (2002) Dehydroepiandrosterone (DHEA) metabolism in Saccharomyces cerevisiae expressing mammalian steroid hydroxylase CYP7B: Ayr1p and Fox2p display 17beta-hydroxysteroid dehydrogenase activity. Yeast 19(10):873-86 {{SGDpaper|S000070219}} PMID 12112241</ref><ref name='S000055653'>Athenstaedt K and Daum G (2000) 1-Acyldihydroxyacetone-phosphate reductase (Ayr1p) of the yeast Saccharomyces cerevisiae encoded by the open reading frame YIL124w is a major component of lipid particles. J Biol Chem 275(1):235-40
+'''Description of YIL124W:''' NADPH-dependent 1-acyl dihydroxyacetone phosphate reductase found in lipid particles, ER, and mitochondrial outer membrane; involved in phosphatidic acid biosynthesis; required for spore germination; capable of metabolizing steroid hormones<ref name='S000055653'>Athenstaedt K and Daum G (2000) 1-Acyldihydroxyacetone-phosphate reductase (Ayr1p) of the yeast Saccharomyces cerevisiae encoded by the open reading frame YIL124w is a major component of lipid particles. J Biol Chem 275(1):235-40 {{SGDpaper|S000055653}} PMID 10617610</ref><ref name='S000114057'>Zahedi RP, et al. (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol Biol Cell 17(3):1436-50 {{SGDpaper|S000114057}} PMID 16407407</ref><ref name='S000070219'>Vico P, et al. (2002) Dehydroepiandrosterone (DHEA) metabolism in Saccharomyces cerevisiae expressing mammalian steroid hydroxylase CYP7B: Ayr1p and Fox2p display 17beta-hydroxysteroid dehydrogenase activity. Yeast 19(10):873-86
- {{SGDpaper|S000055653}} PMID 10617610</ref>
+ {{SGDpaper|S000070219}} PMID 12112241</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YIL124W:''' NADPH-dependent 1-acyl dihydroxyacetone phosphate reductase found in lipid particles, ER, and mitochondrial outer membrane; involved in phosphatidic acid biosynthesis; required for spore germination; capable of metabolizing steroid hormones<ref name='S000055653'>Athenstaedt K and Daum G (2000) 1-Acyldihydroxyacetone-phosphate reductase (Ayr1p) of the yeast Saccharomyces cerevisiae encoded by the open reading frame YIL124w is a major component of lipid particles. J Biol Chem 275(1):235-40 {{SGDpaper|S000055653}} PMID 10617610</ref><ref name='S000070219'>Vico P, et al. (2002) Dehydroepiandrosterone (DHEA) metabolism in Saccharomyces cerevisiae expressing mammalian steroid hydroxylase CYP7B: Ayr1p and Fox2p display 17beta-hydroxysteroid dehydrogenase activity. Yeast 19(10):873-86 {{SGDpaper|S000070219}} PMID 12112241</ref><ref name='S000114057'>Zahedi RP, et al. (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol Biol Cell 17(3):1436-50
+'''Description of YIL124W:''' NADPH-dependent 1-acyl dihydroxyacetone phosphate reductase found in lipid particles, ER, and mitochondrial outer membrane; involved in phosphatidic acid biosynthesis; required for spore germination; capable of metabolizing steroid hormones<ref name='S000114057'>Zahedi RP, et al. (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol Biol Cell 17(3):1436-50 {{SGDpaper|S000114057}} PMID 16407407</ref><ref name='S000070219'>Vico P, et al. (2002) Dehydroepiandrosterone (DHEA) metabolism in Saccharomyces cerevisiae expressing mammalian steroid hydroxylase CYP7B: Ayr1p and Fox2p display 17beta-hydroxysteroid dehydrogenase activity. Yeast 19(10):873-86 {{SGDpaper|S000070219}} PMID 12112241</ref><ref name='S000055653'>Athenstaedt K and Daum G (2000) 1-Acyldihydroxyacetone-phosphate reductase (Ayr1p) of the yeast Saccharomyces cerevisiae encoded by the open reading frame YIL124w is a major component of lipid particles. J Biol Chem 275(1):235-40
-  {{SGDpaper|S000114057}} PMID 16407407</ref>
+  {{SGDpaper|S000055653}} PMID 10617610</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YIL124W:''' NADPH-dependent 1-acyl dihydroxyacetone phosphate reductase found in lipid particles, ER, and mitochondrial outer membrane; involved in phosphatidic acid biosynthesis; required for spore germination; capable of metabolizing steroid hormones<ref name='S000114057'>Zahedi RP, et al. (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol Biol Cell 17(3):1436-50 {{SGDpaper|S000114057}} PMID 16407407</ref><ref name='S000070219'>Vico P, et al. (2002) Dehydroepiandrosterone (DHEA) metabolism in Saccharomyces cerevisiae expressing mammalian steroid hydroxylase CYP7B: Ayr1p and Fox2p display 17beta-hydroxysteroid dehydrogenase activity. Yeast 19(10):873-86 {{SGDpaper|S000070219}} PMID 12112241</ref><ref name='S000055653'>Athenstaedt K and Daum G (2000) 1-Acyldihydroxyacetone-phosphate reductase (Ayr1p) of the yeast Saccharomyces cerevisiae encoded by the open reading frame YIL124w is a major component of lipid particles. J Biol Chem 275(1):235-40
+'''Description of YIL124W:''' NADPH-dependent 1-acyl dihydroxyacetone phosphate reductase found in lipid particles, ER, and mitochondrial outer membrane; involved in phosphatidic acid biosynthesis; required for spore germination; capable of metabolizing steroid hormones<ref name='S000055653'>Athenstaedt K and Daum G (2000) 1-Acyldihydroxyacetone-phosphate reductase (Ayr1p) of the yeast Saccharomyces cerevisiae encoded by the open reading frame YIL124w is a major component of lipid particles. J Biol Chem 275(1):235-40 {{SGDpaper|S000055653}} PMID 10617610</ref><ref name='S000070219'>Vico P, et al. (2002) Dehydroepiandrosterone (DHEA) metabolism in Saccharomyces cerevisiae expressing mammalian steroid hydroxylase CYP7B: Ayr1p and Fox2p display 17beta-hydroxysteroid dehydrogenase activity. Yeast 19(10):873-86 {{SGDpaper|S000070219}} PMID 12112241</ref><ref name='S000114057'>Zahedi RP, et al. (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol Biol Cell 17(3):1436-50
-  {{SGDpaper|S000055653}} PMID 10617610</ref>
+  {{SGDpaper|S000114057}} PMID 16407407</ref>
 <br>
 <br>

← Older revision		Revision as of 20:02, 21 February 2007
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		+	<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
		+	<!--
		+	Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
		+	<ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur.
		+	J Biol Chem 278(5):3265-74</ref>
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 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001386 YIL124W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001386 YIL124W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''AYR1 ''

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 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YIL124W YIL124W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001386 YIL124W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''AYR1 ''
@@ Line 14: / Line 14: @@
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr IX:126204..127097
 |}
 <br>
-'''Description of {{PAGENAME}}:''' NADPH-dependent 1-acyl dihydroxyacetone phosphate reductase found in lipid particles, ER, and mitochondrial outer membrane; involved in phosphatidic acid biosynthesis; required for spore germination; capable of metabolizing steroid hormones<ref name='S000114057'>Zahedi RP, et al. (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol Biol Cell 17(3):1436-50 {{SGDpaper|S000114057}} PMID 16407407</ref><ref name='S000070219'>Vico P, et al. (2002) Dehydroepiandrosterone (DHEA) metabolism in Saccharomyces cerevisiae expressing mammalian steroid hydroxylase CYP7B: Ayr1p and Fox2p display 17beta-hydroxysteroid dehydrogenase activity. Yeast 19(10):873-86 {{SGDpaper|S000070219}} PMID 12112241</ref><ref name='S000055653'>Athenstaedt K and Daum G (2000) 1-Acyldihydroxyacetone-phosphate reductase (Ayr1p) of the yeast Saccharomyces cerevisiae encoded by the open reading frame YIL124w is a major component of lipid particles. J Biol Chem 275(1):235-40
+'''Description of YIL124W:''' NADPH-dependent 1-acyl dihydroxyacetone phosphate reductase found in lipid particles, ER, and mitochondrial outer membrane; involved in phosphatidic acid biosynthesis; required for spore germination; capable of metabolizing steroid hormones<ref name='S000114057'>Zahedi RP, et al. (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol Biol Cell 17(3):1436-50 {{SGDpaper|S000114057}} PMID 16407407</ref><ref name='S000070219'>Vico P, et al. (2002) Dehydroepiandrosterone (DHEA) metabolism in Saccharomyces cerevisiae expressing mammalian steroid hydroxylase CYP7B: Ayr1p and Fox2p display 17beta-hydroxysteroid dehydrogenase activity. Yeast 19(10):873-86 {{SGDpaper|S000070219}} PMID 12112241</ref><ref name='S000055653'>Athenstaedt K and Daum G (2000) 1-Acyldihydroxyacetone-phosphate reductase (Ayr1p) of the yeast Saccharomyces cerevisiae encoded by the open reading frame YIL124w is a major component of lipid particles. J Biol Chem 275(1):235-40
   {{SGDpaper|S000055653}} PMID 10617610</ref>
 <br>
@@ Line 37: / Line 39: @@
 J Biol Chem 278(5):3265-74</ref>
 -->
 <protect>

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr IX:126204..127097
 |}
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 __TOC__
 ==Community Commentary==
 {{CommentaryHelp}}
 ==References==
 <!-- REFERENCES ARE AUTOMATICALLY GENERATED.  PLEASE DON'T EDIT THIS SECTION-->
 {{RefHelp}}